Noncovalent interactions govern an immense array of biochemical reactions in life processes.  A thorough understanding of the subtle energetics of these reactions is crucial to manipulation of these events. The long-term goals of our work are to: 1) investigate the energetics of ligand-receptor binding using the outer-sphere reorganization energy of transition metal complexes and 2) develop an electronic biosensor for the detection of proteins.             Our approach employs small molecule ligands that are known to bind to specific biological targets, typically proteins. The protein-binding ligands have been modified with redox centers that function as electrochemical probes to detect noncovalent binding of targets. We will describe an entirely new type of electronic protein biosensor. A modular, chip-based platform has been developed for a variety of small molecule binding ligands (capture probes). The capture probes provide specificity with subsequent electronic detection of biomarkers as a result of changes in reorganization energy.known to bind to specific biological receptors, typically proteins. The protein binding ligands have been modified with redox centers that function as electrochemical probes of the noncovalent binding event. The environmental variations imposed on the redox center by the receptor cause detectable changes in the electrochemical response. Specific aims include varying: (a) the charge and ligands of the metal complex, (b) the proximity of the metal complex to the receptor and, (c) the affinity of the ligand for the target protein.Finally, we will describe an entirely new type of electronic protein biosensor. A modular, chip-based platform has been developed for a variety of small molecule binding ligands (capture probes). The capture probes provide specificity with subsequent electronic detection of biomarkers as a result of changes in reorganization energy.

Weak interactions: A facile methodology for multiarray electronic detection of proteins

245th National Meeting (2013)

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